Validation of high-affinity binding sites for succinic acid through distinguishable binding of gamma-hydroxybutyric acid receptor-specific NCS 382 antipodes.
Gamma-hydroxybutyric acid (GHB) binding to multiple sites for the tricarboxylic acid cycle intermediate succinic acid (SUC) has been disclosed recently. In order to better characterize these targets, distinguishable binding of GHB receptor-specific NCS 382 antipodes to [(3)H]-SUC or [(3)H]-GHB labelled sites in rat brain synaptic membranes was explored. Eutomer binding parameters suggest identity of the high-affinity target for SUC with a synaptic GHB receptor subtype.
Molnár
Tünde
T
Department of Neurochemistry, Chemical Research Center, Hungarian Academy of Sciences, Budapest, Hungary. tmolnar@chemres.hu
Visy
Júlia
J
Simon
Agnes
A
Moldvai
István
I
Temesvári-Major
Eszter
E
Dörnyei
Gábor
G
Fekete
Erzsébet Kútiné
EK
Kardos
Julianna
J
D000818:Animals; D001567:Benzocycloheptenes / Q000494:pharmacology*; D001665:Binding Sites; D001667:Binding, Competitive; D001921:Brain / Q000378:metabolism; D006885:Hydroxybutyrates / Q000494:pharmacology; D051381:Rats; D017207:Rats, Sprague-Dawley; D011956:Receptors, Cell Surface / Q000378:metabolism*; D013237:Stereoisomerism; D019802:Succinic Acid / Q000378:metabolism*
C039403:4-hydroxybutyric acid receptor; D001567:Benzocycloheptenes; D006885:Hydroxybutyrates; D011956:Receptors, Cell Surface; C066471:NCS 382; C111420:4-hydroxybutyric acid; D019802:Succinic Acid